Number and molecular weights of the basic proteins of rat liver ribosomes

Welfle, Heinz; Goerl, M.; Bielka, H

doi:10.1007/bf00268969

Cited by 26 publications

(4 citation statements)

References 43 publications

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“…They were concentrated by acetone (14). Iodoacetamide was added just before electrophoresis according to the method of Welfle et al (15). The electrophoresis was done according to Madjar et al ,(16), using system I (acidic-SDS) or system III (basic-acidic).…”

Section: Isolation Of Ribosomal Proteins and Two-dimensional Electropmentioning

confidence: 99%

Binding of 16S rRNA to chloroplast 30S ribosomal proteins blotted on nitrocellulose

Rozier

Mache

1984

Nucl Acids Res

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Protein-RNA associations were studied by a method using proteins blotted on a nitrocellulose sheet. This method was assayed with Escherichia Coli 30S ribosomal components. In stringent conditions (300 mM NaCl or 20 degrees C) only 9 E. coli ribosomal proteins strongly bound to the 16S rRNA: S4, S5, S7, S9, S12, S13, S14, S19, S20. 8 of these proteins have been previously found to bind independently to the 16S rRNA. The same method was applied to determine protein-RNA interactions in spinach chloroplast 30S ribosomal subunits. A set of only 7 proteins was bound to chloroplast rRNA in stringent conditions: chloroplast S6, S10, S11, S14, S15, S17 and S22. They also bound to E. coli 16S rRNA. This set includes 4 chloroplast-synthesized proteins: S6, S11, S15 and S22. The core particles obtained after treatment by LiCl of chloroplast 30S ribosomal subunit contained 3 proteins (S6, S10 and S14) which are included in the set of 7 binding proteins. This set of proteins probably play a part in the early steps of the assembly of the chloroplast 30S ribosomal subunit.

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Section: Isolation Of Ribosomal Proteins and Two-dimensional Electropmentioning

confidence: 99%

Binding of 16S rRNA to chloroplast 30S ribosomal proteins blotted on nitrocellulose

Rozier

Mache

1984

Nucl Acids Res

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“…The presence of a high molecular weight basic protein comparable in these respects to protein S1 of the Escherichia coli ribosome [14] has not been observed in studies of other eukaryotic ribosomes (rabbit reticulocytes, [15,16]; rat, rabbit, mouse, and chicken liver [15,[17][18][19];…”

Section: B Conclusionmentioning

confidence: 99%

Ribosomal proteins of Tetrahymena thermophila. Correlation of one- and two-dimensional electrophoretic migration patterns and characterization of additional small and large subunit proteins

Pétridou¹,

Guérin²,

Hayes³

1989

Biochimie

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Further analysis of the protein complement of the cytoplasmic ribosome of the protozoon Tetrahymena thermophila has led to the identification and characterization of seven additional proteins, three in the small and four in the large subunit of this ribosome. Several of these proteins are poorly soluble or insoluble in the absence of high concentrations of urea and are not seen in the electrophoretic distribution patterns of ribosomal proteins in two-dimensional polyacrylamide gels unless 6 M urea is added to electrode buffers in contact with protein samples (first dimension) and first-dimension gels (second dimension). The migration patterns of the 40S and 60S subunits of the T. thermophila ribosome in one-dimensional polyacrylamide SDS gels and in two-dimensional gels prepared by means of the basic-acidic system of Kaltschmidt and Wittmann**, and the basic-SDS system of Zinker and Warner*** have been correlated.

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“…Total proteins (C-TP70) were extracted from 70S ribosomes by the acetic acid procedure [12], and recovered by acetone precipitation [13]. Proteins were then dissolved in 8 M urea and 6 mM 2-mercaptoethanol and further treated with 20 mM iodoacetamide to prevent oxidation [14].…”

Section: S Ribosomes and Total Ribosomal Proteins From Spinach Chlomentioning

confidence: 99%

Identification of an Escherichia coli S1-like protein in the spinach chloroplast ribosome

et al. 1988

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Antibodies directed against E. coli ribosomal protein S1 were used in immunoblotting assays to search for an S1-like protein in the ribosome of spinach chloroplast. An immunological cross-reaction was reproducibly detected on the blots and inhibition experiments have demonstrated its specificity. The chloroplastic ribosomal protein which has epitopes common to antigenic determinants of the E. coli protein S1 was identified as being protein S2/S3.

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Number and molecular weights of the basic proteins of rat liver ribosomes

Cited by 26 publications

References 43 publications

Binding of 16S rRNA to chloroplast 30S ribosomal proteins blotted on nitrocellulose

Binding of 16S rRNA to chloroplast 30S ribosomal proteins blotted on nitrocellulose

Ribosomal proteins of Tetrahymena thermophila. Correlation of one- and two-dimensional electrophoretic migration patterns and characterization of additional small and large subunit proteins

Identification of an Escherichia coli S1-like protein in the spinach chloroplast ribosome

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